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Human Metabolome Database Version 2.5

 

Showing metabocard for Hydroxypyruvic acid (HMDB01352)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:41
Accession Number HMDB01352
Secondary Accession Numbers Not Available
Common Name Hydroxypyruvic acid
Description Hydroxypyruvic acid is an intermediate in the metabolism of Glycine, serine and threonine. It is a substrate for Serine--pyruvate aminotransferase and Glyoxylate reductase/hydroxypyruvate reductase.
Synonyms
  1. 3-Hydroxy-2-oxopropanoate
  2. 3-Hydroxy-2-oxopropanoic acid
  3. 3-Hydroxypyruvate
  4. 3-Hydroxypyruvic acid
  5. Hydroxypyruvate
  6. OH-pyr
  7. OH-pyruvate
  8. beta-Hydroxypyruvate
Chemical IUPAC Name 3-hydroxy-2-oxo-propanoic acid
Chemical Formula C3H4O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Hydroxy Acids
Sub Class
  • Short chain hydroxy acids
Family
  • Mammalian Metabolite
Species
  • ketone
  • primary alcohol
  • carboxylic acid
Biofunction
  • Component of Glycine, serine and threonine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 104.062
Monoisotopic Molecular Weight 104.010956
Isomeric SMILES OCC(=O)C(O)=O
Canonical SMILES OCC(=O)C(O)=O
KEGG Compound ID C00168 Link Image
BioCyc ID OH-PYR Link Image
BiGG ID 34120 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01352 Link Image
Metagene Link HMDB01352 Link Image
METLIN ID 482 Link Image
PubChem Compound 964 Link Image
PubChem Substance 7885304 Link Image
ChEBI ID 30841 Link Image
CAS Registry Number 1113-60-6
InChI Identifier InChI=1/C3H4O4/c4-1-2(5)3(6)7/h4H,1H2,(H,6,7)
Synthesis Reference Behal, Francis J. Hydroxypyruvic acid formation in Aspergillus niger. Archives of Biochemistry and Biophysics (1960), 88 110-12.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 208.99998 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.43 [Predicted by ALOGPS]; -1.5 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • mitochondria
  • peroxisome
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
General References
  1. Kolvraa S, Rasmussen K, Brandt NJ: D-glyceric acidemia: biohcemical studies of a new syndrome. Pediatr Res. 1976 Oct;10(10):825-30. [PubMed Link Image]
Metabolic Enzymes
  1. Serine--pyruvate aminotransferase
  2. Glyoxylate reductase/hydroxypyruvate reductase
  3. Putative hydroxypyruvate isomerase
Enzyme 1 [top]
Enzyme 1 ID 6069
Enzyme 1 Name Serine--pyruvate aminotransferase
Enzyme 1 Synonyms
  1. SPT
  2. Alanine-- glyoxylate aminotransferase
  3. AGT
Enzyme 1 Gene Name AGXT
Enzyme 1 Protein Sequence >Serine--pyruvate aminotransferase 
MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEI
KEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIG
ARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLL
LVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSF
YLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHG
RLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLR
IGLLGCNATRENVDRVTEALRAALQHCPKKKL
Enzyme 1 Number of Residues 392
Enzyme 1 Molecular Weight 43011
Enzyme 1 Theoretical pI 8.55
Enzyme 1 GO Classification
Function
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function L-serine + pyruvate = 3-hydroxypyruvate + L- alanine
Enzyme 1 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 1 Reactions
  • L-serine + pyruvate = 3-hydroxypyruvate + L-alanine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 36582 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P21549 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SPYA_HUMAN Link Image
Enzyme 1 PDB ID 1H0C Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1179 bp 
ATGGCCTCTCACAAGCTGCTGGTGACCCCCCCCAAGGCCCTGCTCAAGCCCCTCTCCATC
CCCAACCAGCTCCTGCTGGGGCCTGGTCCTTCCAACCTGCCTCCTCGCATCATGGCAGCC
GGGGGGCTGCAGATGATCGGGTCCATGAGCAAGGATATGTACCAGATCATGGACGAGATC
AAGGAAGGCATCCAGTACGTGTTCCAGACCAGGAACCCACTCACACTGGTCATCTCTGGC
TCGGGACACTGTGCCCTGGAGGCCGCCCTGGTCAATGTGCTGGAGCCTGGGGACTCCTTC
CTGGTTGGGGCCAATGGCATTTGGGGGCAGCGAGCCGTGGACATCGGGGAGCGCATAGGA
GCCCGAGTGCACCCGATGACCAAGGACCCTGGAGGCCACTACACACTGCAGGAGGTGGAG
GAGGGCCTGGCCCAGCACAAGCCAGTGCTGCTGTTCTTAACCCACGGGGAGTCGTCCACC
GGCGTGCTGCAGCCCCTTGATGGCTTCGGGGAACTCTGCCACAGGTACAAGTGCCTGCTC
CTGGTGGATTCGGTGGCATCCCTGGGCGGGACCCCCCTTTACATGGACCGGCAAGGCATC
GACATCCTGTACTCGGGCTCCCAGAAGGCCCTGAACGCCCCTCCAGGGACCTCGCTCATC
TCCTTCAGTGACAAGGCCAAAAAGAAGATGTACTCCCGCAAGACGAAGCCCTTCTCCTTC
TACCTGGACATCAAGTGGCTGGCCAACTTCTGGGGCTGTGACGACCAGCCCAGGATGTAC
CATCACACAATCCCCGTCATCAGCCTGTACAGCCTGAGAGAGAGCCTGGCCCTCATTGCG
GAACAGGGCCTGGAGAACAGCTGGCGCCAGCACCGCGAGGCCGCGGCGTATCTGCATGGG
CGCCTGCAGGCACTGGGGCTGCAGCTCTTCGTGAAGGACCCGGCGCTCCGGCTTCCCACA
GTCACCACTGTGGCTGTACCCGCTGGCTATGACTGGAGAGACATCGTCAGCTACGTCATA
GACCACTTCGACATTGAGATCATGGGTGGCCTTGGGCCCTCCACGGGGAAGGTGCTGCGG
ATCGGCCTGCTGGGCTGCAATGCCACCCGCGAGAATGTGGACCGCGTGACGGAGGCCCTG
AGGGCGGCCCTGCAGCACTGCCCCAAGAAGAAGCTGTGA
Enzyme 1 GenBank Gene ID X56092 Link Image
Enzyme 1 GeneCard ID AGXT Link Image
Enzyme 1 GenAtlas ID AGXT Link Image
Enzyme 1 HGNC ID HGNC:341 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q36-q37
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Nishiyama K, Berstein G, Oda T, Ichiyama A: Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase. Eur J Biochem. 1990 Nov 26;194(1):9-18. [PubMed Link Image]
  2. Purdue PE, Takada Y, Danpure CJ: Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. J Cell Biol. 1990 Dec;111(6 Pt 1):2341-51. [PubMed Link Image]
  3. Takada Y, Kaneko N, Esumi H, Purdue PE, Danpure CJ: Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. Biochem J. 1990 Jun 1;268(2):517-20. [PubMed Link Image]
  4. Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ: Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase. Genomics. 1991 May;10(1):34-42. [PubMed Link Image]
  5. Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A: Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. Biochem Biophys Res Commun. 1991 May 15;176(3):1093-9. [PubMed Link Image]
  6. Purdue PE, Lumb MJ, Allsop J, Minatogawa Y, Danpure CJ: A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. Genomics. 1992 May;13(1):215-8. [PubMed Link Image]
  7. Minatogawa Y, Tone S, Allsop J, Purdue PE, Takada Y, Danpur CJ, Kido R: A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. Hum Mol Genet. 1992 Nov;1(8):643-4. [PubMed Link Image]
  8. Danpure CJ, Purdue PE, Fryer P, Griffiths S, Allsop J, Lumb MJ, Guttridge KM, Jennings PR, Scheinman JI, Mauer SM, et al.: Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. Am J Hum Genet. 1993 Aug;53(2):417-32. [PubMed Link Image]
  9. Danpure CJ: Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. Biochimie. 1993;75(3-4):309-15. [PubMed Link Image]
  10. von Schnakenburg C, Rumsby G: Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. J Med Genet. 1997 Jun;34(6):489-92. [PubMed Link Image]
  11. Amoroso A, Pirulli D, Puzzer D, Ferri L, Crovella S, Ferrettini C, Marangella M, Mazzola G, Florian F: Gene symbol: AGXT. Disease: primary hyperoxaluria type I. Hum Genet. 1999 May;104(5):441. [PubMed Link Image]
  12. Basmaison O, Rolland MO, Cochat P, Bozon D: Identification of 5 novel mutations in the AGXT gene. Hum Mutat. 2000 Jun;15(6):577. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13057
Enzyme 2 Name Glyoxylate reductase/hydroxypyruvate reductase
Enzyme 2 Synonyms
  1. Glyoxylate reductase/hydroxypyruvate reductase, isoform CRA_b
Enzyme 2 Gene Name GRHPR
Enzyme 2 Protein Sequence >Glyoxylate reductase/hydroxypyruvate reductase 
MRPVRLMKVFVTRRIPAEGRVALARAADCEVEQWDSDEPIPAKELERGVAGAHGLLCLLS
DHVDKRILDAAGANLKVISTMSVGIDHLALDEIKKRGIRVGYTPDVLTDTTAELAVSLLL
TTCRRLPEAIEEVKNGGWTSWKPLWLCGYGLTQSTVGIIGLGRIGQAIARRLKPFGVQRF
LYTGRQPRPEEAAEFQAEFVSTPELAAQSDFIVVACSLTPATEGLCNKDFFQKMKETAVF
INISRGDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLKNCVILPHIGSATHR
TRNTMSLLAANNLLAGLRGEPMPSELKL
Enzyme 2 Number of Residues 328
Enzyme 2 Molecular Weight 35669
Enzyme 2 Theoretical pI 7.44
Enzyme 2 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • L-serine biosynthesis
  • L-serine metabolism
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • serine family amino acid metabolism
Component
—
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID Q5T945 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q5T945_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID AL158155 Link Image
Enzyme 2 GeneCard ID Q5T945 Link Image
Enzyme 2 GenAtlas ID GRHPR Link Image
Enzyme 2 HGNC ID HGNC:4570 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 15963
Enzyme 3 Name Putative hydroxypyruvate isomerase
Enzyme 3 Synonyms
  1. Endothelial cell apoptosis protein E-CE1
Enzyme 3 Gene Name HYI
Enzyme 3 Protein Sequence >Putative hydroxypyruvate isomerase 
MAPLRFSANLSWLFPELSGLPARVRAAGSSGFEAVEVAWPYAETPEALARAAREAGLRLV
LINTPPGDQEKGEMGLGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADRIA
VKAEMEAVFLENLRHAAGVLAQEDLVGLLEPINTRITDPQYFLDTPQQAAAILQKVGRPN
LQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGRGEPSSPGELNFPYLFQLLEDE
GYKGFVGCEYQPRGDTVEGLSWLRSYWDRRGHPEAGQ
Enzyme 3 Number of Residues 277
Enzyme 3 Molecular Weight 30406
Enzyme 3 Theoretical pI 5.19
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 Specific Function Hydroxypyruvate = 2-hydroxy-3-oxopropanoate
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID Q5T013 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name HYI_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AY775560 Link Image
Enzyme 3 GeneCard ID Q5T013 Link Image
Enzyme 3 GenAtlas ID HYI Link Image
Enzyme 3 HGNC ID HGNC:26948 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available